ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A928B0J8 | MSTQNVNDEKEMTFGEHLEELRKILMRVVIVFVILFIVMFAVSNIWLKILMGPQNANFPTYQFLAWMGDVLGSEALKISPDNFELINTRMAGQFLLDMKCAFIGSLIVALPYLLFELWLFVKPAIPPHLRRKCMRYTIETPVWFMGGLLFGYFVIVPLTINFLTHYSVDAPIANMITPDSLISTVMGVAMAGGITFLLPMFIRLIATMGLITADTMRNYRRHAAVALLIFAAIITPPDVFSQVLIFIPCYFMYELGIRIAARIDAQRAKAMANVPATTPAVAVEDDDEVEDRETVRYDD | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Location: Cell membrane
Sequence Length: 299
Sequence Mass (Da): 33793
Location Topology: Multi-pass membrane protein... |
J2F078 | MASHGLILALALLVGSSVSVHAEPLDEPLKPLPPVPALDPKRVQLGQRLFNDPRLSINNTLSCASCHRLDKGGADDKALSLGFDGKPVEVNTPTVFNASLNFHQFWDGRVDTLEEQVHTVVISPTEMGNTWETVVKRIADNSGYAKDFSEAYPEGVSEASIRSALADYERTLQTPHSRFDQYLQGNTDILTPREKFGYQRFKEYGCIACHQGVNIGGNMFQKFGVMGDYIQDRGNPTRADEGRFNVTGDEADRQVFKVPSLRNVAITAPYFHSGSAPTLERAVEVMFKYQLGREPAGKDTELIVEFLKTLTGEWEGKPL | PTM: Binds 2 heme groups per subunit.
Cofactor: Binds 2 heme groups.
Subcellular Location: Periplasm
Sequence Length: 319
Sequence Mass (Da): 35304
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A0A5N9EED1 | MTSLKISASLLASDFTQLGSDIGEIESSEANELHFDVMDGQFVPNITIGIPILESIRPITKLPIDLHMMVVNPENHIEAFSKAGGNIFTFHAEACENIHKTINSIRKTSMSVGISIKPETPVEIIYDFIDYVDRILVMTVQPGFGGQQFMPETLPKIKKIAELISKNKRHIDLAVDGGIKKGTVELAIKAGATTLISGTGLFGHKNGVGAGISDFFQYIESSKSN | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Carbohydrate degradation.
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 225
Sequence Mass (Da): 24431
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A0A975DI87 | MTILIEQNAWTKPVVAVSGAIVLTFATFALMQHLISRDNSRPLVSEIMPVAVLLSAHTDSEVKEKSKVLTPPPRMKPMPPRATEVPEETSSTAELGVIDAGNIHIDTVLTRDFGQPSNYDANPIVRITPNYPIQAARDGLEGWVKLSFSISEIGAVVDAKVIGSEPAKIFDREALKALKRWKYRPKVQNGSAVIQENQTVVLEFSLSN | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A0P7WXQ2 | MIPDYVQRGDYEPLDRLIDLALLEDIGTGDVTTQAIYSGTEHARASVVAKQDGIIAGLAVAERVLRRVDQTLVFTPSVQDGQRAANRQSIGEIQGKAGSILTAERTLLNFIQRMSGIATMVHGYVEAVAHTSARILDTRKTLPGHRVTDKWAVLLGGGVNHRIGLYDRYLIKENHIAVAGGIDQAIRACLVHRNTLARTVEIELEVTSLTELEQALVHHKHIDYIMLDNMSVDAMKTAVAMTGGRCRLEASGNVTIDTVRTIAETGVDFISIGAITHSVPAMDISLLFS | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1.
Function: Involved in the catabolism of quinolinic acid (QA).
EC: 2.4.2.19
Sequence Length: 289
Sequence Mass (Da): 31416
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A0A0P7WK51 | MFTGRIVKSTGSWYLVEKSDGSGIISARLPGKMRLEGLQQTNPVAVGDLVDLQSVDDGTALVRNIHPRSNYITRQATHGKRGEQILAANIDVGIVVQSVRQPQFKTGFIDRFLVTCEANHVTPLIVINKLDLARGKDMERLDEIRNLYTSLGYDILLMSVERQDSVKQLKERIQGSIVTMTGPSGVGKTSILNALHPELNRTTAAVSGFSNKGKHTTTFAEMLPIGNNTYVVDTPGIREFGLVDIDAPGLSNFYPEMKDLRTACRFYNCTHVHEPGCAVMQAYDEGTIHPDRYMSYLQIIESLS | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyz... |
A0A928AG50 | MRSILLYFGSFNPIHKGHIALAEWVVEQGLCDELIFIVSPQNPFKEQEGLAPEFSRYEMCELACKASRYPEQIKVSAVEFVLEKPSYTINTLRYLRENFGSEMKFSILMGADNIENFDKWREYEEILRDYPLLVYPREGYSVERFADKITFLENAPLFDFAATDIRKSIAEGEDFRDKLSAEVAHYIIQNKLYK | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
W9G531 | MVEGLRLMAVHAHPDDESSKGAATTAKYVAAGASVMVVSCTGGERGDILNEKLKNDPHILRDIAQVRRDEMEAARAVLGCEHTWLGFVDSGLPEGDPLPPLPEGCFALEDLDVTTEALVRVIRSYRPHVMTTYDEKGGYPHPDHIMCHTVAMSAFEAAGDPERYPHAGEPWQPLKIYYNGGWSKDRLTAIHDAMLEGGLDSPYAEWLANWRPRRHGRVTTRIACSDYFETRDRALMAHATQVDPDGFWFQVPLAIQQRVWGVEEFEAAVSYVPIPEEEDDLFAGLGTLAEADALATTRGLEIAYDGRISPDAEPEQEEDG... | Cofactor: Binds 1 zinc ion per subunit.
Function: A mycothiol (MSH, N-acetylcysteinyl-glucosaminyl-inositol) S-conjugate amidase, it recycles conjugated MSH to the N-acetyl cysteine conjugate (AcCys S-conjugate, a mercapturic acid) and the MSH precursor. Involved in MSH-dependent detoxification of a number of alkylatin... |
A0A1B9F3M1 | MIIVADVGGTNTRLALFKGGRIEEIKIYPSNSFRSFEEILSEYLKTIGHYDCEAISIGIAGTVSGSKANCVNLSWGIEIEALQMAFDIPKVVLMNDFEAAAWGVIALSTSDLLKVGGKETRANSPRAILGAGTGLGEAIIIPCNNQRFHVLPTEGGHTEFAPCDETEWHLFQFLKEKYGHVSIERVVSGPGLKDIFLFLSGNEVSPQTVVELALQKRDENAMKALEIFIKNYGKEAANLALKSLAFGGVYIAGGIAPKIKEVFAEFGFRDAFEDKGRMKAIVRDIPVFIVLHPYLGLLGAGIRLIHVPT | Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
EC: 2.7.1.2
Subcellular Location: Cytoplasm
Sequence Length: 309
Sequence Mass (Da): 33627
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A0A132SF46 | MATLQFRMMDSPVGPLTLAGRDGRLRHLRMVDQTYEPSRDGWEPDDEAFPDAVEQLEAYFAGDRTEFELDLDLVGSEFQRRVWAALLTIPYGETRSYGEIARQIGSPGAFRAVGLANGHNPIGIVVPCHRVIGANGSLTGYGGGLDRKRALLELEKNRVSPVATLFD | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
W9G659 | MSTDARDHTLDHTFDHSPGHSPEQPGGHVLDDLLSRAADLDANAPLSGIRDRFTLPEGVIYLDGNSLGALPTAVTEVVHDVLERQWGERLIRSWNEADWWGAPTRIGDALGRLVGAATGQIVVTDSTSVNLFKALMGAARLRPGRTVVLTDPDSFPTDLYMTDSAARLAGLEVRRVHPRDAVRAIHEAGDSLALASYSQVDYRTGEKWDLVSITEAAHAVGALACWDLCHSAGAMEVDLDAGGADLAVGCGYKYLNGGPGAPAFLYVAQRHLADFDQPLTGWHGHARPFEMGPSYAPAEGIARGRVGTPPLISMLALEAA... | Pathway: Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.
Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
EC: 3.7.1.3
Catalytic Activity... |
A0A926ETY7 | MVKRIRVLQWYETNPYRNLALEEYLLDQLPAGECILYLWQNRHTVVIGRNQNVWKECSLALLEEEGGYLARRSSGGGAVYHDLGNLNFTFLAHDEDFDVEKQQEVILNALKKMKICAVKSGRNDLTVNGCKFSGNAFYHKGGRSLHHGTLLVDVNIPSLSKYLTVSSEKLRSHGVSSVRSRVTNLKNYCPKLTVDLLRQRLVGSFEEIYGFSAAPILEQEICMQEVEKLYEKYCSQSWKFGRKITASYTLEHRFAWGGIQIKALVKGGLIKEAAVFSDAMQAQWPSQFEQALTGSLFSSQAMAQAALQTPQTDELTRKMA... | Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
EC: 6.3.1.20
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+)
Sequence Length: 332
Sequence ... |
A0A843AU67 | MSSISAGDLEKFCYCPLSWKLRDAEGGGAALVEGSVLHQRMAGELEEIVKGERRASVYETWVIAFSVLATAMALIGVFVFASSDLELRGRVLSILALVWTLLAVLVMYATARARPPRDRERGEVVVGVAAIMAMVLALNAVPIFGISTDHGLMVQAIALVLLMGASAALVMSQRQRDRTKRARQNTKVQGRIAYIGEGGSPRLLISERHGLTGRPDYIVEIDGDLVPVEVKTGRVPRGPLFSHVIQLAAYCLLLEEQEGRVSYGILRYGDVEHIVAFDENLRSLLLKKVAEMREAVASGEAHRDHDRPGKCRSCSRRSAC... | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences ... |
D3FDW4 | MLTVGVLALQGDFAAHARMLAELGAQPREVRVPADLAGLDGLVIPGGESTTMTLGIEREGLAEPLRELARGGTPVFGTCAGLIMLDRAHLGIMDVLATRNAFGRQVHSFEEDLTIAGVEGPSVRAVFIRAPWVAELGDSVEVLAAVDGHPVAVQQDHLLAISFHPELSGEPRLHERFLALVESARSARTSR | Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
EC: 4.3.3.6
Catalytic Activity: H2O + L-glutamine =... |
A0A0Q4AXU5 | MANEIKIRKGFTIRLVGQAEKVFKRLPLAGEYSLYPDDFPLLVPGLLVREGDTVLAGSPLLCDKRDPRVRFCSPVNGRVARIERGERRHIDRVVVECDAKDSLEYKDFGAALPATLSCDDIIAKMLQAGVWPMVRQRPFNIVASPDVRPRAVFISAFDTAPLAPDLDFAIKDDGESFQVGVDVLRMLTDGGVHLGVNAKYPPNIAFEEARGVTLHRFSGIHPAGNVGVQIHHVAPVAKGEVVWTLHPLDVVVIGRLFSTGHYDARRIVAVTGSRVAKPRYYLSMVGMPIRTLLDGQLQEPEEKLRIISGNVLTGTKVGLN... | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
EC: 7.2.1.1
Catalytic Activity: a ub... |
A0A8H6SG94 | MQVVARQNLRRVVPRLARCVNTQTPESGPKTTSFGFRTVPEDEKEYLVKNVFDSVASKYDLMNDASSLGVHRLWKDSFVSGLRPGRRGPLRCIDVAGGTGDIALRILDYAREHYADRETTVEVVDINDQMLKEGFRRFKKTMYHNTPQISFHEANAQELPSEKFADNSYDLYTIAFGIRNCTSIPAVLREAHRVLKPGGTFACLEFSKVNNPLLSLAYDQYSFTMIPLLGTILAGDRASYQYLVESIRKFPPQPEFANMIREAGFSTGERHGWSVYNVKPISLQTLMHLPLFISIAQSLWVVGAAVTRQSQHPLVAADHS... | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Catalytic Activity: a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S-adenosyl-L-methionine... |
A0A0S8GE21 | MGSVLGIPVYVDYSWLIIFVLITSTISQEYVRSHPAWQPSQHVLAGVVTSLLFFMCVFLHEMGHSLVARVFGIPVLSITLFLFGGVAQIRREPRKPAHEFLIAIAGPLTSGALSVVFFILSLITATVVNLPIVSSICFWLAGINLMLAIFNMIPGFPLDGGRVLRAIVWAVSGRFEGATRIAAGIGSFIAYFFIAMGIYLAITYKPFIHGLWIAFIGWFLLTAARSSLVQLVTRRAFAGLRVRDIMEQIPQRVSPAMSVQALVDGPILQHGLRSFVVEDGGVLRGLVTLHEIKATPRQQWENTPLQSIMVPARDLVVVDP... | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 369
Sequence Mass (Da): 40767
Location Topology: Multi-pass membrane protein
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A0A8B9GDV3 | MKFTRVLCFTNSREASHRLFLLVRAFGGVSVAEFSSLLPPNERQRTIKEFEQGKIQLLISTDATARGIDIKAVNYVINYDAPQFIRTYIHRVGRTARAGKVGVAFSLVLRIQERRFLRMLKDAGIQDIKKHPVKGNSLKPLVQRYEEALCNLEKTIKVMEMGKEIANHD | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 169
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 19303
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A0A1L7FBU3 | MGWVQDYEPVGGLWVSALLAAAPIVVLLAALGVFRRSAHLSAALALLTALGIAVFSYGMPVGLAGNAALLGLIFGIWPIAWIAFHAVFFHNVTVATGRFESIKAALAGFSPDRRIQALLIAFGFGALLEGVAGGGSPIAITAAMMAALGFPPIKAVVLALLANTAPVAFGGLGNPMIVLGSVTAPLLGVETEEATQLFSAMSGRQLPFLALIIPAFMVVVLAGWRRMVEVWPALLVTGGSFAITQFLISNYVSPSLVDVGAALAAMGSLWVLTRFWRPREVWRFAAEDAEAEGADAARQAESTGPGPRRTRADATSVPGA... | Function: Uptake of L-lactate across the membrane. Can also transport D-lactate and glycolate.
Subcellular Location: Cell membrane
Sequence Length: 603
Sequence Mass (Da): 62413
Location Topology: Multi-pass membrane protein
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A0A1F0FT51 | MAVGIRNFAYDHRLVSSWKSEIPTICVGNLSVGGSGKTPHIELLISLLKREYKVAVLSRGYGRRTRRPIIASLEDNADRIGDEPFQIKQKHPEVMVYIDGDRRRALETMEAMPEEERPDVVLMDDGFQHRKVTPSFSILLTPYCKPYYDDYLMPYGRLRESRKEAARAEAIILTGTPRQVNVTEMRLKMDNLGTMAYQDVFCTSVRYEQPRPLFTEADTTSRHRLTQDSPILVVSGIARPAAFQQTCKSTFPKVVDYIEYPDHHRFTKEEVEVLVDDLQSDQDLFVLTTEKDGMRLLTCQQWIPKEVRNRIWILPISIDI... | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A1F9R4D8 | MKVLLLGSGGREHAIAWSLSRSPLLTKLWAAPGSDAMAALAERVDLEALDPDAVARFARENGVELVFIGPEAPLAAGVGDAARAAGVPVFGPSKAAARLETSKAFAKDFMARHAIPTARSLCCEGTAAAKDAARALGGKCAVKADGLAAGKGVIVCRAFPEAEAAVDLLCATTAGKTLIVEELLDGPELTVMVLTDGRACAVLPPSRDHKRLHDGDQGPNTGGMGALAPAPVPAGTWKRIMDEILAPTMAGLTDDGLDYRGALYAGIMLTQAGPKLLEYNARFGDPETQAVLPLLDADLLTLARDCAMGELIAGVIPAKP... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Len... |
A0A1Q3E7W4 | MVERDLIDALCKMKGLKHFTWRHDAGPVLHEELWSTLKDLGVSSLRFIDRKACDFVGDSGYYRSIFESPTFWTFAKLTSLELETSFLAGLDAEDDMKYMPSLIKLLENNAETLEAFNLSFRDPDALVDVTSILSQVTFTRLREITFRRASCTPQSLSKFLSGHPSIVSLSLSPMMAGRRWEQLSVSADSLPNLMHLNCSPFHAGKILDGSESSPRPLFCLTGIDVRQTIKLSDYFDVDKQDAYADDEEIAEIDTYEAEQLITAPWKDELFSKLKSSKQITHVALNETDGPKDLEVLAELMPQIRWIDVGTKRKDAAASKE... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer r... |
A0A1G3PHG0 | MNNPVVDHIRLEGETLVLLDQRLLPGEEKYLRIRTSEEVFDAIRTLAVRGAPAIGVAAAYGIYVHLANFKSARETEALRAEAERAVEYIKSSRPTAYNLFYALDRQLQVIRASESSDRMLDGLRTEALSIHREDLESSERIGEYGAEFISDGMGIISHCNAGGLATGGNGTSLAVIFRAQRDGKKIKVYVDETRPLLQGSRLTAWELERAGVPYEIITDSMAGDVMRKGLAQAVLLGADRIARNGDFANKIGTYSLAVLAKYHGIPFYTAAPASTFDLSLANGGGIVVEQRSREEVLGFAGIRTSPMGAKAYNPAFDVTP... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
EC: 5.3.1.23
Catalytic Activity: S-me... |
A0A8C5E5D1 | LKHNEFTSRYKEEKLLGEGGFSQVYAGECRSTSTPVAIKHISKKDVQLVKVNCQGNVYDEILEVFLMEQAAGRLCDGSFENPAVIGLMDVFHLETEVIIIMERPPDTVDGFDYLFEIKHIPEDQVKVIFKQIINAALLMHKNGVFHRDWKLKNILVNRNNGTPEIRVIDFGCGDFVENEPFSRFYGTPAYAPPEFFRGETYKAEATTVWQIGVMLYITCTWTAFYTSVYMKKDKEVLENVSMECNDFLSQCLALDPNQRPTLEDLLLHPCVFHILKHMNPVLYDISCRTS | Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation.
EC: 2.7.11.1
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Length: 290
Sequence Mass (Da): 33280
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A0A0P7ZAY9 | MPDSLNHIFSEPANLATAWSAFFTNELYRCGLRHAVISPGSRSTPLTLAMAAHPHIQTHVVLDERSAGFMALGIGKASGRPAALICTSGTAVANYYPAVVEARMSGVPLLVLSADRPPALRQVGANQAIRQQGIFGSYTVFEHDAGEPVARTEDFRRLEILAGQAWNSSIHHGGPAQVNFPFRKPLEPTAAFRDYLPGHYTESLEARTEPLTRSAPVQWRPPAAVFQTIARSRRPVIIAGTLPAHCLLPEILDMLSDEGIPLLCEAGASSGRQTGEAYITGFNAFLRSASVRDRLQPDLIIQIGPGPSGKGLEHYLREYR... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting s... |
A0A5M4EPM5 | MKIVIMGAGAVGSYYGGVFKRNGIDVTLINRGKHHEAIINNGLNIRSFWGDYNVDVNASNKTSNLGTFDVVFLTTKLYSNQEAIKQLSNLCSDKTIIITIQNGVSSYEELSKFFDSANIIPAATYIEAEIISPGTILQKGSSVVIEIGEIDGNFSERLNNIKNKLSFEELEINISKDIKASLWKKMISVGAFGTIMTSFRSSFGEIISSMYGEEVLRGTMNEILEIGKLDGVNLNDVDIDKVVHGLKEESDSITSSMQQDLTNSKPLEIDNILGHVVVLSKKYNYPTPFSTTLVSSLQKFKEG | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 303
Sequen... |
A0A3D6B2R7 | MKILVINCGSSSIKYQLLDMRSEEDYSLLAKGNLEKISLPDSKITHKPTGKAPVVKCMSVPDHTKGMQIVLSMLTDPTCGVISHFDEIDAVGHRIVQGADFFNGSVIVDEDVMEKIKICCDFAPLHNPAHILGIRAVQSVLPKVPQVVVFDTAFHQTMAPKNYMYALPYEYYEKYRVRRYGAHGTSHQYVSHEGAKVAGIDINNSRIITCHIGNGSSVTAIKNGKCVDTSMGFTPLEGMIMGTRCGIIDANIVPYIMKKENLTPDQMTDVMNKKSGFIGLSGKSSDMRDVVGFAEQGDSRSQLVVDKLVLDITKLVAAYI... | Cofactor: Mg(2+). Can also accept Mn(2+).
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
EC: 2.7.2.1
Subcellular Location: Cytoplasm
Catalytic Ac... |
A0A1J0LJC9 | MTTKKIAIQGIKGSFHDEAAHILFNTQPIEIIECFTFKDVAKSIINNEADYGIMAIENSIAGSILPNYNLLIEYNLKIIDELYMPINHYLMAQSGQKIEQIKEVNSHPMALMQCENYFEPYPKIRMVEVADTALAAKRIVDQDLEEIAAIAPKRSANVYGLEILGEKIQTVKNNFTRFFVIQKDEHSISHFNKVSIKFKVSHESGSLAQILNQIAFRRINMSKIQSVPVIEEPWNYAFFADLILDEGSEFDTFLESVRPLVKDLKILGKYQNKRTL | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 276
Sequence Mass (Da): 31548
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Q6NDK6 | MVPVLSVENLSVSMTNRDGDLVPVLENLSFTVQKGRTIALVGESGCGKSMTALAIMRLLPEGFVVTGGRIVLDGEDLLTARPKRMRALRGDAMSMVFQEPMTALNPLYTVGDQIAEVLYYHRRLSRKDAAEQAVQFLKAVQIPAAEQRAKAYPHQMSGGMRQRVMIAMALACRPKLLIADEPTTALDVTVQAQIFDLLAQLQDETEAAIVLITHDLGAVAELADDIAVLYAGRCIETGPAHEIAARPRHPYTRGLLGCVPHLTIGVAKPEEWVDLGEIPGMVPALGNRGPDCAFLARCANASEACRSRPQPPLGTIAAGH... | Function: Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Subcellular Location: Cell inner membrane
Sequence Length: 332
Sequence Mass (Da): 35721
Location Topology: Peripheral membrane protein
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A0A8J5R5M2 | MKLFCQVLKLIHFIVTALIIVYDYLITIKEDLINYLRPKTLKCIDTIVDVCDVSKLEKLPNHLVIVVASKDKVSFSDLAKIVGWCCTLGIPNITFYDREGIIYEKSELLINEFNKLTPSFVSRVIWSNKITRKFNTKANGEFKQYTRVNFSVYNDGKPEIIKLTRELSQAVKLKLLKTDDINYDLINEKLSLPVPDPDLAIITGRTFSTFGLLPWHIRLTEFYNVPTHHNISPHKFIQILEEFAKCHQRFGT | Pathway: Protein modification; protein glycosylation.
EC: 2.5.1.87
Catalytic Activity: (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-trans,poly-cis-polyprenyl diphosphate + n diphosphate
Sequence Length: 252
Sequence Mass (Da): 29181
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A0A1Q7TPQ6 | MKRALILLVSYALIAACPITSSQGQNSSSAETKTAIFAGGCFWCIQPAFDKARGVIKTAVGYCGGTEPNPTYEVVSSEKTGYRESIQITYDPAKISYDQLLDIYWRQIDPTQADGQFTDIGPSYRAAIFYGNDGEKKVAEASKEKLARSGKFNKPIVTEILPAMKFYPAEAYHQKYYQQNPEHFEAFEEGSGRVSFKKKTWENKEPQRP | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
EC: 1.8.4.11
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionin... |
A0A524I2C8 | MDRELLLKGSRRLGWAEAHMSVLREIGERLEKNESLRGVKVGMALHVEAKTGMLAVTLAKAGAKVRLASCNPLSTDDSVSLALKEERGIEVYARRGESNTEYYENLNSVLDMRPDFVIDDGADLITMLHTVRREQLEEIKGGNEETTTGVIRLKAMARDGKLKFPVMAVNDARMKYLFDNRYGTGQSTFDGFMNATNLLIAGKELVVAGYGWCGRGVAMRAKGLGANVIVTEVDPIRAIEAKLDGFQVLPMMQAVRQADIIITVTGCKDVVRKEHLSVIKDGCVLGNSGHFDNEISKKALEEVAAPPVRVREQVERYDLT... | Cofactor: Binds 1 NAD(+) per subunit.
Pathway: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Function: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
EC: 3.13.2.1
Subcellular Location: Cytoplasm
Catalytic... |
A0A840RMG4 | MYAPRYLLATIALASAFAIADEPVCQGRNDLPRVLEHVCYSGQPDATSCPYHDDAFGIFENNRAPYHYLLVPRQKVCGIENEALWQSGTHDWFAEAWRLRHLFAEAKPVSGGVPLERVGIAINSIPGRSQGQLHVHISCVEQGVAKQLAVHASQFNDTWQPLDLTTPDGVQHYLARRLAGPQIDPDVFASLAKAHPELAADKGNITAFAASVADGSVIRPLVLIGHYSDHNQGHAEDLLDGCGNVQAAPKPQQ | Pathway: Lipid metabolism.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + CMP + 2 H(+)
EC: 3.6.1.26
Subcellular Location: Membrane
Sequence Length: 253
Sequence Mass (Da): 27523
Location Topology: Single-pass membrane protein
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A0A259PI94 | MAYPLHRPAPSAPSSQSEPLGVPASPDLPALEQDVLAYWKADGTFVASVEAREAGPDGSNEFVFYDGPPFANGLPHYGHLLTGYVKDVVPRYQTMRGHRVERRFGWDTHGLPAELEAERILGITDKSQIEEMGIAAFNAACRESVLTYTHEWEDYVTRQARWVDFEHDYKTLDPTFMESVIWAFKQLYDKGLAYSGYRVLPYCWRDQTPLSNHELGMDADVYRDRQDQTVSVTFPLVGERAEALGLAGVRAVAWTTTPWTLPTNEALAVGADITYAVVPAGPAGTSAGTGPFLLARDLLPGYAKDLGYAAPDDAVAAVSR... | Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves ... |
A0A928AG22 | MTVRLIIHKIRDAVESLYGKHEAEAIARMVVCNKLNYNLSQLVVRYDEECEVEGLERMVAELKSGRPVQYVLGEAEFCDMVFEVQEGVLIPRPETEELVYRIVETAPRSVRILDVGTGSGAIAISLANMVEGARVAAVDISKEALAVAQRNAERLGAEVEFVEADALGDMSHLGEFDVIVSNPPYIPQSDIAEMRKNVVDFEPHTALFVPDDDALKFYRSIARNARTMLAEGGVLWFEIYEKFGTEMCEMLYDEGFAQCGVEVDANDKARMVWAKL | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
D0JA95 | MIFDLSDYRKNYHKNSLLESEVPKEPFQLFHDWFQQEKLFNIHKKNNEEINAMSISTIGEDGVPETRVVLLKEYSEKGFIFYTNYYSFKGKSIQNRPRVCISFYWKNTERQILIKGITSKIKKEKSDEYFQKRPKENQIGCWASRQSSTVSSKEYLLKQYKKWYNFFKNKTIKRPFDWGGYIVKPYKMEFWQGQTNRLHDRLVYSLEKEKKWILYRLSP | Cofactor: Binds 1 FMN per subunit.
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
EC: 1.4.3.5
Ca... |
A0A5N9DRQ4 | MKKNDINKFVLKHIQQIKPFDPAEPLDSMAAKVGVEPEKIIRLNANENPYGPSPMVNETIKSLQANIYPDPEQNAIRTELSKFTKMPKETILCGAGSDELIDLLFRLFCTPNNNVIECDPTFGMYSFCARITGTSIISVPRDDNFELDINAVKSAITPETRIIFINSPNNPTGNLAQQKDIEILLETGLIVVIDEAYYEFTDKSFAPLVLTHNNLIVLRTMSKWAGLAGLRIGYGFFNQDLVEQLLKIKQPYNVNSAAELALMASLKDVDYLMNNVKLIVKERSRLYSALQEFGSYIKPLPSEGNYILCESLKVPSSKVV... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 363
Sequence Mass (Da): 40683
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A0A5N9GR35 | MSTGHPQRVQSMFDRIAKRYDAFNTVASFGRDEAWRRLAVRLAAPEHVDRALDAASGTGKLAAALATQATHVTALDFSNPMLQRSMPLLAAQGLSTKVASIQGDVLALPFPDATFYCATIGFGLRNLDDIPAGLAEFKRVLKPGGRLVVLDIVKPKNIVSKAVYTIGFRGMLPLVGWALSGSRTAYQYLPNSVQRYLTPPELVAEMTDAGFRDVSYRNLMLGSIALHSGKV | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquino... |
A0A6A6HMW2 | MDIRDSASSQSASSHTSLPRRRPSHTQSQFSNFPRSESFRQLPPVLQNYILPSSAASSRDSESSPTIRPTFEGSSYDSIQLPSFAEITGFRDTTGSPLGFDQSQPSLSWSDLLDPGSESDYLGMAPRKAPKRAAEASSSSPNKRMRKDSVPGLQRNADRSIEELDLVEEDTALADTLKKQRQQQVALQEDSRKPTKLSKISCIICMETPTNLTATSCGHLFCYECLMQALNFSARNGGDGRRGMCPVCRKVVSRVKKDDIIPLEIMKKGLATQPKRSSSSGT | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 2... |
Q54PB0 | MANLNQSSSSIQVPKLSKYMISFGYFLMGIIVTATMFLSNNNNFSIVSYTLLSEIIFGVIISFLHIGFSIFAFPGNSSTLDKINRSLIGLSIGNFVFYFLLILYGAPFLKSIHTTFFFGFLLSSMCCLPPSILLGLNPQNWKDLFFTPNHNNIIDTCTTILVVFSILGAWIGAFPIPLDWDRPWQQWPISCVFGSIVGHIFGLFICSVYSLVHKEKKSM | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 219
Sequence Mass (Da): 24572
Location Topology: Multi-pass membrane protein
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A0A139MWH9 | MKQLKERFDALSDAIVAIVMTILVLEIAVPATTKELPYLLEEIALFLVSFVIIINFWYRRFQAMRATETTTFRTFVMDVIAHAILSLYPLATKMLVEFNIKWIAIIFFGGINLATAFLINRMTYELATQTIKNLVDKDDERIHMLNDWLKRRTLVSLISDIVMMLIALCFNTVGVYIYILTPFLEFIGIFKRGRVMEAAFHEGQTFKEIVEHRAAVENLQERHENIKQRQQIHRQEVAERHAEHQKRHSKNHKSKKH | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 257
Sequence Mass (Da): 30131
Location Topology: Multi-pass membrane protein
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A0A1L7F9K8 | MAKILCVLYDDPADGFPPRYARDDIPTIDRYPDGQSTPTPEGLDFRPGELVGSVSGGLGLRNFLERAGHEFVVTSDKEGPDSVFERELPDADVVISQPFWPAYLTSDLIAKAPRLRLAITAGIGSDHVDLKAAVENKVTVAEATYSNSISVAEHAVMQILALVRDYLPAHRLVTDDRGWHIADAAQRSYDLEGMAVGVMAAGRIGVAVLRRLAPFDVTLHYTDKNRLPIELEEELNLVFHEDVRSLASAVDVLSIHAPLHPETKGLFDDELIGSMKRGSYLVNTARAAICDRDAVVRAVESGRLAGYAGDVWYPQPPPAD... | Function: Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.
Catalytic Activity: formate + NAD(+) = CO2 + NAD... |
A0A1W5XUU5 | MGAGRGRGAAAPGDRAPRDEGAPACHRGGEAGRPLQGRPRPNRRPGARWRRYEAGGATAVSMLTERRRFGGSAEDLAAVRARVTLPVL | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 88
Sequence Mass (Da): 9271
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A0A1Z5HUA3 | MSQEQKKGSKKRWLWIGLLVVLILLLTAGQTYFITTRFLSHQTETVRTPNGQEFRKFTLEPFTVNLADLNFRRYIRLTIVLEYQDKRLSKELEEKRHRIRDTIINFLWTKKVSDFASAGKVDSIREQLLEKINQSLITGKLTGLYFEDLIIQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 152
Sequence Mass (Da): 17979
Location Topology: Single-pass membrane protein
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A0A2T2UJP6 | MILACASSALSQKVSSIPACAVPAPATASPTTDPTLLTPTTATVDLDAVRHNARLIQRRTAPTAALMAVVKADAYGHGSVRVAQALQDEGVEHFAVARVSEAVRLREAGIEASILVFEAPLPEHLPAYARYQLDVNVCSKAVAGALVQLAEQRPPSEPPLRAHVKVETGMERLGNKPEVAAGIAGRLRRTDGVEVAGLWTHFVSADDPEQQAFTRRQLGILQEAADSAGPLPNGRVHAANTPAMLHFAESFRRLDPTFVRCGLALYGLARFPPSVREALGDDLRPAMRFTSKITHLKTVDEGATVSYNRSWTAPERVRLA... | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 487
Sequence Mass (Da): 51961
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A0A8C5GW34 | EYLGVTLLTLIRLFYPLRCNCTTCEKQGYECETDGACMASTSFIQGKEQHVRICIDQENLVPAGQPFFCLSAEGYLNTHCCYVDYCNSIDLKVPVSGPTWGPVELVAVIAGPVFLLCVLLMVGVFLFQYHQRAYSHRQRLEVEDPSCDHLYLAKDKTLQDLIYDMSTSGSGSGLPLFVQRTVARTIVLQEIIGKGRFGEVWRGKWRGGDVAVKIFSSREERSWFREAEIYQTIMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYSVTIEGMIKLALSAASGLAHLHMEILGTQGETDDFTPTHLDGTK... | EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 327
Sequence Mass (Da): 36909
Location Topology: Single-pass type I membrane protein
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A0A938HS25 | MLQDDIRAAIDLGTTKVSAIIGKQRDGGSVEVLGMGTAPSDGMTRGAITDAPQVTGAIRTALSAAEKDAGVSIRAAYVGLGGSQIESRNQWTRVPNQGIAVVTQTDVNRALAIARSEAANSGDHLLHVLPRSYALDGIYGVRNPLGMHAREMYIQTHVITGAREAMGLLTSTVEDAGLQVGGTIVQMLGSAESALNRQEKDDGVVLIDVGGGTTDVAVFYEGTIVHTVVLPVGGWQFSNDLVQSFNTSFAEAERLKITHGAAIPAVRGATDELSVNANGMDQPLVITRRELSQLIHDRASEMLEMVRLRLQAPHLRDIPL... | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 428
Sequence Mass (Da): 45355
Location Topology: Peripheral membrane protein
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A0A1G3BV25 | MQYEFKNKKITVMGLGLFGGGVGVAQFLAKQGARVTVTDLRNASELSPSLKQLEGLPISYKLEGHDEEDFIKADMVIVNPAVPKNSKFIQIARNNRVLIDTEINIFFKLCPAQIIGITGSNGKSTTTTLTGKILEETQRRTWIGGNIGKSLLGCLDEMKPADIVVLELSSFQLEELNHTKKSPHLSVVTNISPNHLDRHTNMDEYIQAKKAIILHQGSGDYAILNYDDPELRRWEKDCKGHVLWYSAIHTPANGAFIKCNDIVLSVNGQNTTIPCVSSVKIPGIHNLQNVLAASCAAYLSGARKQHIEKAITTFTGLEHR... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
A0A6A6HJT5 | MATFSIAAALLGLASSVSAHGQVQGIVANGEFYEGYSPSFQYSNPPPTVIGWSIPQDLDNGFVASSALQTDDIICHVNATPAKGHAVVAAGDVVELQWSAWPSSHHGPVIDYLANCNGACETVDKTKLEFFKIDGVGLVNDNPVPGTWASDQLIANNNSWVVTIPKSIAPGNYVLRHEIIALHSAGSAGGAQMYPHCINLQITGSGTTKPTGTLGTALYKEADPGIEVNIYQSLSYVIPGPSPIADAVSMKQS | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secre... |
A0A7Z9HRS9 | MSELATLARPYAEAVFDSAQASKTTEKWSEMLAFLAVVMSDERMADLSNNPKVSLEQLTTLMQDICGKQLNPQGTNLLKLLIENRRLTLLSEISRLFEERKADAEGYIGVSVKTAFALTKAEAKKLAEVLEIKLNKKVHLEMTIDKSLIGGFLVHAGDTVIDGSIKGHLQQLANRL | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A6A6H971 | MTSSSTSTADYRDYPKHIINQSYSPHSNLNNLDIILLRPYDRNDISKIWIVYIHGGAWRDPRKTKSGISASLPHLYASAAASHIAGIASLNYRLSPHPTFPVKPGDSADLAARSAQHPTHINDAIDALRWLKTEWGVRDGGYVLVGHSCGGTMAMQIMTSEGRKWKTREQVKALSGEKGEEGKDTPMPRVVMPVEAITDLPKLVANHAEQNMYEDFVVGAFSKEREVWEEASPTKGTYRGEKWRDASLVILAHSKEDELVEWEQCDLLLDVLKAQGWKEKGSQIEADGKVSKEPGVRVLELRGKHDEIWEDGRELSRAIN... | Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic ac... |
A0A2J0Q827 | MFLDKFICKQYVIYDNLNFTHAFNCEWHKNYFTIFKQIKNLIDLVLNTQTDDKKYDRKFFYGLLETAVHEVIPFVDKISVSINLVGTSRIKDLNKKYRGKNKITDVLSFPIHSAKDFRNSDSFNGIRKEVDIGKEKHAIMDLGDIFICLPVIKKEAKREHLSKGGFLNNPAKDEKAVEEILRHKLAQMTVHGFLHLLGYDHHSPEEENEMFGLQDKIINNIVL | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 223
Sequence Mass (Da): 26016
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G5H6L1 | GTGPRNGGENRRRSAGHSGNCCKKQPRRQRPPTATAGSATLPGTGRRTAAITVLVTGANGQLGNEMRRIAATDATTAPATTPPTATAGSATLPGTGRRTAAITVLVTGANGQLGNEMRRIAATDATTAPAAATAPGNVRYLFTDVAELDITDPQAVRRTMRENDVEVIVNCAAYTNVNKAEEDEATADLLNHRAVANLAAAARERGATLIHISTDYVFGGDGNVPRREDDPVRPLGVYGRTKLAGEKAIAEAGCAALILRTAWLYSEFGNNFVKTMLRLTAQTPRVKVVFDQAGTPTYAADLAGAIHRMISSGAYRGNEG... | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 406
Sequence Mass (Da): 43233
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A0A1Q2D3M8 | MGKKLRIGMLGLGTVGTGVVELFENYRYKVQQITGLDSCLAKVFVRNSHRKKALAERHHLTLVTDMAEIINDPTIDVVIEVLGGIEPAKTAISQALKSGKHVVTANKDLMAQCGIELQQLAKENACALYYEASVAGGIPILRTISSSLSSDAIEIVYGIVNGTTNYMLTNMTISGLTYQEALLEAQRLGFAEQDPTNDVEGIDAVYKMIILTQFAYGMTIKIDDVTRQGITHVTASDIQSARKLGYVIKLIGTTLITKEGVAVDVAPVFIAKTHPLASVSNEMNAIFVKSTGIGESMYYGPGAGATPTATSILSDVLTIA... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 427
Sequence Mass (Da): 46502
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A0A5N9B2I0 | MVNSRTIAIDGPVASGKSTVGSLVASQLSWQFVDTGLMYRAVAWLLSKKAIKKTNLDKIKTILDKHQIETTCDNEKTTITIDGDIVNDYLSDPSVIKTVSEFSTIPYIRTYLVKKQRNLSEISSTVMAGRDIGTVVLPNASTKIFLQAGIKTRTTRKLSILEQNDEESQKSITNEISHRDKIDSNRKISPLKAASDSFVIHTDNMNLKQVVNTIIDLNSYNK | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 222
Sequence Mass (Da): 24692
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A0A5N9GTD8 | MTTSNQPDTQRLFIAVELPPDTLAALSQLIHGLRASALQGMSLVAAKNIHLTLKFLGNVNTDQVPGLMSTLDSLASKAASFTLELGDVGGFPNLKRTRVLIVCMAGDMQPLEKLVNLVEDACELIGFARDKRPFSPHLTVARMRDSASPEDRTKAGEVLTSLPWSSGLPAPIDSFKLIKSTLTPQGPIYETLHTVALPLS | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 200
Sequence Mass (Da): 21501
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W5TCQ3 | MSEAKNTGPRRDTETLSHLDDEGRARMVDVSAKAKTARTAVAAGVLRTTPEVVALVRADDMPKADVLATARIAGIAGAKKTSELIPLCHQLALSSVHVRFDFTDDAITIEARAKTKGPTGVEMEALTAVAIAGLTLHDMVKAVDPAAVLDGVRLLTKDGGKHGHWERLGEPVDHATSGRSSHAHDHTRPGQAQTAAPSPGASADTPAGHGPSGRPHDSAHGAMEPTPAPLATAAHSGRPSEPVDDAAAHSGHAHGRGPGTHSGVARAGEGSRSAVVVVASTGAAAGTRVDTTGPVLMDWLAGLGFSVRGPLVYADAEIAA... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
EC: 4.6.1.17
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diph... |
A0A369W6R7 | MIRRLLELVGSVLPVFLIAFLVLVVAADVFARNILRVPFYAAHDLAILAFSASVWLGLIGAALYGQLFGIGFFVELLPERLRRVVVVLSHIIVIIIAVAVIQAAIAQITTARFTTFLALGWPKWIVAAILAVGMGGIIIVQLVAIVEIFRGEGADA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 156
Sequence Mass (Da): 16788
Location Topology: Multi-pass membrane protein
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A0A8H6SXB9 | MLSQPATRVVGRLFKSPSIKLEHYYRYAHTIPATADDRALKEVFDQSRGTQSSSGPPTGLFGHRTLTSPDALFKLADATVLRAQLLTKRILRARESRRELSLVIKNIDRLYSLVAGVTNAAELIENSHPDEKWAEAAGAVHRRLRDYTNTLNGHAGILAVQTEVLDNPSLMKSFSPETRATALRFARDELETSPRRIRKSSALSTKISSLGLKYLHGAVEYGDPPRILPAHLEGLDDWLGFPDGLPEDGIIVNPGSQEAEIIMRIGPDAEARRQLYIASNTSPPGQIETLHSMLRARGQLARVSGKSSYAEFALMNNMLK... | Cofactor: Binds 1 zinc ion.
Function: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing b... |
A0A1Q3EAI4 | MSSEIDKLLVTLTDPAARKGFEMEMLSFKQMFSRYNSGKEQGTKLHWAEISPPPAGQLVMYDSLSLQADLTSLNKLAVLKVNGGLGTSMGIKGAKSALEVKNGLTFLDLIVQQIQHLNTTMHIDVPLVIMTSFQTQADTIRVIKKYANDSVRVLTFNQSRYPRILRDTMLPCPRTAEDEGRSWYPPGHGDLFMSLRRSGVLEQLLSEGKEYLFVSNSDNLGGVVDTAILQHFIESDLDFLMEVTNKTKGDLNGGTLVNYDGTLRLLELGQVPFEHIEDFKSVFNFKIFNTNNLWINLKALKRILDNEGLDLDIIEKTRNL... | Function: Plays a central role as a glucosyl donor in cellular metabolic pathways.
EC: 2.7.7.9
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Length: 469
Sequence Mass (Da): 52558
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A0A1H1WXJ8 | MSTATADHQTASAGRRNGATTGRRLAPHPDRLLPPDPGVRAIARSIYSSVAGAPIYSPHGHVDAALIADNRPFGNPAELLITPDHYVTRLIHAHGIGLDQLGVKNPDADPREIWRLFCSHWDVFAGTVVRYWFESELSEVFGITDVPSAETADQIYDQLTEQLAKPEFHPRELFDRFNIAVLATTDDPSADLAAHKTLAADPDFHGAVVPTFRADRYMSPDVTGWKGYLDELGQAADIDTGSYAGLIDALKARRAYFKECGATASDSGMPDAYAEPLPDAECERIHQAGIAGTVTAEDAAAYRRNMLYQLAAMAAEDGLV... | Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 5.3.1.12
Catalytic Activity: D-glucuronate = D-fructuronate
Sequence Length: 492
Sequence Mass (Da): 53786
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F6KE92 | GWTVYPPLASNIAXGGSSVDLAIFSLHLAGXSSILGAVNFITTVINMRPKGMTLDRMPLFAWAVVITAVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
K2L681 | MHSVNEILTLLSNNSLLLLMIALLGERYFTLPLHWHPLTLFNLLATYMSAKVNRDNVQQQTLAGLLSCVLLLILVLVPLLIFRWAADLPQLVDLLLLYVALLYQPYRHWLATAAVAIERGHKRRARALMSRLTARDCESLSEPGLVKSWVELRWYYALNYRLAPILAWLLGGIALLLVVRVLVQLHHLWPRYIPRYRHFGQAPAMLTQWLMWLPYQTVNLLLWLTHRDSRWAVADSHGWWLAQARQQQLLAQRTRSSLGGPLRYRQQRYSRARFNAGRQADRQLLRQERKMLMYLGRAATLVITLLLIFSLVYNQKPW | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 318
Sequence Mass (Da): 37228
Location Topology: Multi-pass membrane protein
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A0A7S4RZI0 | AHAPAPRGLRTRGGADAAAMGAPPRGRAGAGLRTGEQAAEAGANGWVRAGLCTACGPRAFNEDAHVLLCDWAPEPGPGRGPAALFAVCDGHGGSAVARWTARKLAEELRVELDEGKAWCEEETRRTAAECAFLALDRGLLRSMGAAASTCGATCVAAAVCRLPREAACARAATSGDDHERGRSSSRSRSPRRMPAATGDEEVGLSRVLLMNVGDSRALLCRQGVGVVKETADHKPDAPAELARIEASAGFVSAAKGQDPARVDGVLSVARALGDFRWKLDASRPPEAQRISPLPDVYDLEVQGGDVLLLACDGVFDVLSS... | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 372
Sequence Mass (Da): 38347
Location Topology: Peripheral membrane protein
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A0A2Z3YX12 | MNARSPRSPVTRAPSPTVVRDDADHLEIITGVLVIGGGPAATWAALNAARTSAGEGLGVTLVDKGYCGASGVAATSGVGHWLTPPGSPLRDETFRIKNATGGGQSDRVWVDAVLDETWAQISTLPAMGWDRVDRNRRQPSLDLTTDNPSGAPYFRGPAPDYLRFLRGQVKKAGVTVLDHSPAVELLVTDNRDAVVGARGLQVRAGRNWTVHAHAVVLATGGTTWRSHSLGGDTNTGDGQLMAAEAGADLAAMEYSNFQGMVPFGTSMDKNGYFIKAEYWTGDGTPIHYDDLHYSRVPLLEHSVKGTVYARFSQFAPAQRA... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.
Function: Catalyzes the oxidation of L-aspartate to iminoaspartate, the first step in the de novo biosynthesis of NAD(+).
EC: 1.4.3.16
Catalytic Activity: L-aspartate + O2 = H2O2 + iminosuccinate
Sequence Len... |
A0A0S8GH17 | MINVMKMTDATMIDDTLNRTGHSVRQHTLAQGTSWKGPTRKGAGAITLHLHPAEADSGIWFLRTDLDVNRRVIAARWDAVAETRPALTLANRDGVVLRGATTLLAALRVRGIDNALIEVEGPEVPSRPSDFESYLELLIHAGAQPQALPRKALRVQQPIEVRDSAGIATLIPARDFRVQLIVPRAEADPTAALLDASLVSDLTEPAAQATAGGLRLEASAVPLHELMRLPFALRVRLISVLGHLSLAGPPLIGHFTGYRSGTTLHHTLLRALMTRLTASYLTVDQHRMHRNEPTGIAGSIDNSSRPNKDYH | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6.
Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step... |
A0A7T3CJE2 | MITAALALPLILAVVLVLSGIAKLRAPQTVAAGFRDLRVPAALDRAWLRALLPWGELVLAAALLAAPGALAPVAAIAAALLFLAYWVLIRRALSFEKPVSCGCFGEASAEPVSGWTLARNTVLALVALGWVACSFVTSGPGLIAALRGADALWLLGGALGALTLWLSMPRGAAAPAAVDPAAGAGTLGAPRPAGAPGEASADQEAEDYVRRPTPGMLLRDASGELISLRSLASQGARLLLLVSPGCGSCTITMADAVQWRGNLGPVTLHLMTQAPQESLEAQTDASLHEDALYDVGGFAYELLGMAGTPTAVLVGADGAL... | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 370
Sequence Mass (Da): 37662
Location Topology: Multi-pass membrane protein
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A0A1Z9NMS4 | MKPIKALGIATLLNEKVLDVFYFEISESDQSKNSITRLDEDVYSKLVHLKDLKIAENKEVIEVNLVEDVKIQDVPTAFLKLHLISLKQFKPNELNLDNIFNVLETLAWTSKGPMTVKEAEKELLVSKANGSDFKINSIDKFPPLTNYVLPEKVRIADTARIRLGAYLGEGTTVMHAGFVNFNAGTEGPNMIEGRVSSKVFLSKGSDLGGGASTMGTLSGGNDQVVSIGENSLVGANSGVGISLGANCIVEAGLYITAGTKVTLLDDENKEIKTIKALELSGVSNMLYLRDSVSGKVIGKSNNTNFSLNEILHVNN | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3.
Function: Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA.
Catalytic ... |
A0A351KWI8 | MSESLLWFDYETFGLDPARDRPAQFAGLRTDPDLKVIEEPFTVFCRPPIDYIPNPESCLLTGISPVHAMARGVPEHEFIRQILAAYAVPGTCGVGYNSIRFDDEVTRNTLYRNLHDPFAREWQHGNSRWDLLGVVRMARALRPEGIVWPRDKDDRPTLRLDHLTIANGIEHEDAHDALGDVRATLELARLVRHAQPKLFNYLWELRSKRAVLSLVEPGSMTPFLMASTRMSSETQNLGIVVVVGRQPENPNALITYDLRFSPESWMQDHPALEGERGPFGVLHINRSPALAPMSVLRSQDEARLGLDVLMHMRHLGELKQ... | Cofactor: Binds 2 Mg(2+) ions per monomer.
EC: 3.1.11.1
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Length: 468
Sequence Mass (Da): 53043
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A0A7D4XNC3 | IFGAWAGMVGTSLSILIRAELGHPGAFIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLTLLISSSMVENGAGTGWTVYPPLSSGIAHAGASVDLAIFSLHLAGISSILGAVNFITTVINMRSPGITLDRMPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPIY | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
W9BSN6 | MLKRLAIATGWARRTRRSPALRIGIAIAAFVVGVGGRLALDAYLTGVPYITLFAAIVMAAFFAGFWPAMLATVLGAITLEVLIMPSVALARPDDMNWLPTTLFLLTSLMISLIIESVFRAHDDRLAVAEKLAQLNAGLDGLVAERTAQLEQQIAERQVAESRLHQAEKLDAIGHLTGGIAHDFNNMLAIITGSLDLAKRRLGGQVDPRIVSHIDNAANAAERAAALTHRLLAYARKQPLDPRRLDINALVGSVHALLERTLGEQVVVDLQLDADVWPCLADQTQMETAIINLAVNARDAMPDGGKLVIETANVTLDDRYC... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 546
Sequence Mass (Da): 59220
Location Topology: Multi-pass membrane protein
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A0A1L7F8R4 | MTVLGCADSRVPPEVLFDRGFGDLFTVRSAGEVLDDAVVGSIEYGVEHVGTPLVAILGHAQCGAVAAAIDTVNGEGHLEGDISSLVRDVEASVRATPADSDADAFLAACVATQARRVATMLLERSEIVRDAVEHHGVQVVTAVYELETGQVNRLD | Function: Catalyzes the reversible hydration of carbon dioxide to form bicarbonate.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 155
Sequence Mass (Da): 16241
|
A0A524I593 | MEMTVAWRKILNLLRISYTLPFVMASVTGAAFALSVSDGLLLAFLIPLDVFFLAMFVNISNDYFDHKSGTDASRFQFRTPELEEALKEIYDERVYWTGNTFDKGEVSERNGRMIIGIIALGALLVSIPIIMHGGWLVIILGAVAFFLSYFYTAPPLNLGARGLGELDVGMSFFMMSFFTYYVIVQIWSWEMFLIALTVGLTVMLMRFVDQMSGYKAHLEGGEKDWCVRLGLERAVSAVGILLVVLYAFCFALIYFDPLYVVLFLTLPMSFGLMRMLRNKEDDLRFIRPAPQMFKLALGNQILIIISLILQSVLPWTIW | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 318
Sequence Mass (Da): 36130
Location Topology: Multi-pass membrane protein
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A0A524IYF1 | MLTGILLTGGHSTRMGRDKGLLKLGQKPMVLHVLEEMSGIVDEMVVSVGVGRKGDYEPIFAGKARITEDSKDDFGPLEGIRAAVSSSNSDLVAICPCDTPFVRAKIYKLLLEESEDTEGAVPIIRGFPEPLHAIYNRNAVERACTKVVERGGFRVSEMFQSMDLRFVQEKRIREVDRELSSFWNLNSPDDFRKAEMILAESDLEKSSFSLAHTT | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A8H6W1I7 | MKFSSSCLDTDTKGDEMASQPQHTTFLERNAQYVASFGDKGSLALPPARKLAIVTCMDARLDPEAHLGLKEGDAHIIRNAGGVAKEALRSLILSQRLLGTREIAVFHHTDCGMLTFTAPDVQAIIKDAAPGNAEIAARVEAIDWLDFKDLEKAVKDDVAYLKSEPLILEGTPVTGWVYDVGTGKITQVA | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 189
Sequence Mass (Da): 20407
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A0A0A1UKZ0 | MEDAPLPPPSTSRTPRPRLPSQPSHGHTNPRSQRLTPLGPSVHSSSVVSNQTSRLAPLSPGSQELRDINEDYLDYESNSVFRVDSDYTLTATTTHNVSNKRTASLSDEDDSEDRGPLLSEYMCPICYSPPRSAIVTLCGHILCGQCLHGATTTRQTAVRPLCPVCRTPLPNLRFAFPSIQFNLNPNIPLNVMNENRASGAGVDVNAVQERWDPARSGVIGLEILTVNEM | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 2... |
A0A351KV65 | MALIQGQWAGFDEVGRGCLAGSVIAAAVILPEN | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 33
Sequence Mass (Da): 3358
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A0A343K4L5 | MKMMVIFLLSXXXXXXXXXXXXXXXXXYGGLSLVISGGIGCGIVVSLGNVFLGLIVFLIYLGGMLVVFGYTAAMATEEYPESWVGNLVAFSMLVFAFLTELLWYMMSGEILAVYNMELLDSLGNYCVGQDWNGVSWLYGCGGWALVLLGWVLFMT | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 ... |
A0A351KRM6 | TDVVNIGIGGSDLGSRMVVKALTPYVDPGLRVHFVSNVDEADLIQTLRGLDPETTLFCVASKTFTTLETMANAKSARDWLLNQVKDTSAVARHFIAISTNTVKVAEFGIDTANMFEFWDWVGGRYSIWSAIGLPIALALGMDRFEAMLEGAHRIDEHFRTAPFHRNIPVIMGLLGIWYDNFFAADAYAILPYDQYLEYLADYLQQGDME | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 209
Sequence Mass (Da): 23365
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A0A7S4PSX8 | MASVQRSPAAAAVASKAEAGAGAGGGRRSRSRSTPMRSALWLEEPVRSVGAAGGDTQAAGRPRPSGSQSVSRQPRSRRCREESPEQQAVKRRKKSRSTRRDQAALQPRRRIESKNVPKHSAHGPRTPTTDPGSRTAEGPPRSVGHGGVHLQATPETAGTPGPPQFPEGSAVRVHGLKHKEENNGREGVVLGFVTGKQRFRVKLTGGTCHNFKPDNLEEIRKQAVEPAPSTTAEPADGAAKPQPAASAQPDPVGVAHEAGPLPRGRAENGSLADTSSQSPERRASGPPTSGGALREVDQAAWTLPAPAPRPLPPMGSLPPA... | Function: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
EC: 2.7.1.160
Catalytic Activity: 2'-phospho-[ligated tRNA] + NAD(+) = ADP-alpha-D-ribose 1'',2''-cyclic phosphate + mature tRNA + nicotinamide
Se... |
A0A6V8LIY1 | MKRTGVHVFLVLWALVVTVPLLWAVVSSLKTDSQIFTSPWSVPTDPQFGNYARAWGQAQIGTYFLNSLIVVGGSVLLVMLLGSMTAYVLACYRFRGNRLVYYLFVAGMTFPVFLALVPLFFVVKQLGLLNTYPGLILVYTAYALPFTVFFLRGFFRNLPWAVAEAAIVDGCSHYGVFFRVMLPMAKPGLVSIGIFNFLGLWNQYLLPLVLNQQPERYVLAQGLAALAVNQGYRSDWSALFAGLTIAIMPVLIVYLIFYRHVQAGLTAGPSSDHAALVHRREIGHLPALGDLRRPGRGRVVVVLLRRRVLCGLHGAGGGVH... | Function: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
Subcellular Location: Cell membrane
Sequence Length: 690
Sequence Mass (Da): 76538
Location Topology: Multi-pass membrane protein
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A0A6F9WZ89 | MTTHPFSDLPSHFQYILKHRPFRYAIAALLVGAAYMTRLNYFYWFGHRAPFVTFYPAVLLAAWYGGLLPGILATVLSAAIAIYYVIPPVHSLWLHDQVDIVLLTVFIVFCGLVSGSMELMKRYRQRVDERTAELARAVDSLREESAERALALEELREKDRLIIQQSRLAAMGEMISYIAHQWRQPLNNLGLLVQQLKVYNDMSNLHELDIGENVAKAMQVIQHMSRTIRDFSDFFKPEKSRTDFNVSEAIRKTVGLLEAGLASQNVTIHIRENGQMPYCNGYENEYAQVILVILQNAKDICAERRIKDPTITISIAAVNG... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 389
Sequence Mass (Da): 43657
Location Topology: Multi-pass membrane protein
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A0A1G3PJ70 | MNVLTVFLITAGALMAIGVFGILTRSNIIKILLSINILQTGVNLLLIALGYRDGGAAPIITSQVSSAVAMVDPLPQALVLTSIVIAFGTTAVGLVICLNYYMTHKSLDVHTFGNEEREHQQKEVVD | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0A8H2VFH0 | MSVHDSNEHDIWASGNETKSPWGANESNEANHKTTTTALNQNSNVSSTLNSLTIDNENPGHSIFGSSSPVGSETNIFKDSLDEQQQENDSEEQGVWGGSNKSAKFPPFSDPLTATLNIFDDNITRGEGSSEVNNIETEQQTNNEELEEWIKAARKRYNPLLSDIVSIEEIPEREGLLFKHINYKLVLSIELPDTEPSDSKSVVRRYSDFDWLQEVLLKRYPFRMIPELPPKKIKTSQNLDPTFLKKRQHGLYTFINLIMKHPILKEDDLVLTFLTVPTDLSTWRKQLNNKFDTVDEFHNKRITKTFIKMWKPELSIHLND... | Function: Required for vacuolar protein sorting.
Subcellular Location: Membrane
Sequence Length: 552
Sequence Mass (Da): 63817
Location Topology: Peripheral membrane protein
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A0A385D5Z9 | MSAGKPRGARSRGAHTSRRTTGRDGPRSREVKDAEALTKTWRSPLVTVTAARAPLPIHPPVPLTCNNTKTVVAPREFRDWLGALRDQAELLRAAGYFVMVPALMLSLTREVLSGTGIAYGGQDCAAESESVTGETPASHLADFGCTCVMLGQQQRRQLRGEDSATVAAKAARAGEAGLVPVVCAGEAEHCPPAEAAETVATQVRLVMDQLPATAPLVVLYEPHWASPAHQAADARHVGAVQRGLDALRAGRPGVVRTLYGGAVTPGTWTALRDGTHLDGLHLGRAGIDAAVRAAVVSEILADPPAGRAGGDGSVS | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 315
Sequence Mass (Da): 32782
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A0A7S4QVI2 | KPYLAESPTPVCKGMEPVDISRVAGWRRSEQGKSSSAQSTRCLQRSPHQAPGLCARDPLPSRPNQRSPALAPFLVVAGVCLLSCELATVPWRLAAWTSSPPRRQGASSPPTPFRGTARAAGSPALQADGAGADVATLRLDAATPVVDPLREPSADGEGADADRQPSDQKAHEALKSAEEKMKLKNEKIQKIKHLRSQLSAVQSEIAKCQEQKDECIKFKQSLEKLTPQELRAVHRMDADAGEKAGATLPPDATMADLLPNLPRNSKEVLAYRGIRNPSPIQAIAVPRLIEGLSAVVHSETGSGKTLSFLLPALERVRKVD... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 806
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 87213
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Q55D94 | MGISNNKKQAVDGANQQQTDKYPSKSGLPPTIGNGPMEKYEPKDEYIRVDSMQQHWIRRKLISDKYPEILNLPTNHTPTAFWVIGLVASLIITAKLLENSPIWLIVVVAYIFGATVSHALWVLIHELTHDLVFEGSFMNSVFLLIADLPHIVPAGVSFRHFHRLHHSFLNETYTDPDVPVPFENKLFGHSIVGKAIWFCLYSIVIACRSVFYPLKNQSPFSMWLVANYICNITFTYVIFQWVGVYGMTYLVLSSLMSVGFLLHPLGARWIAEHFAVTQSEQETYSTYGLINTIGFNIGYHNEHHDFVRVPYVYLPTLTKV... | EC: 1.14.19.17
Subcellular Location: Membrane
Sequence Length: 361
Sequence Mass (Da): 41502
Location Topology: Multi-pass membrane protein
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A0A385M9H2 | TLYFIFGIWSGMVGTSLSLMIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLILLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMKPNGMEFDKMPLFVWAVGITALLLLLSLPVLAGAITMLLTDR | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A2Z6A9V7 | MEQQRCYAAGQSPLWSSNDVTQQGSRPLWSSNDVTQQGSRPKTKLAIKGVKLKISLISAVSENGVIGSGPDIPWSVKGEQLLFKALTYNQWLLVGRKTFDSMGVLPNRKYAVVSKNGISSSNENVLVFPSIENALKELSKVTDHVYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDIKFPIMPENFNLVFEQFFMSNINYTYQIWKKG | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Sequence Length: 208
Sequence Mass (... |
G8XUG4 | MGAECCKRIRCELCPQASNTLTDVLGRRVDLGPYDVLSSSEGEGEEEDDEKDDSIDGDDDSVTRSPGHLKKPKGGGSGYMPPTVQITAKCTRGSGKDKKTLLRAPTPKPKRKGVRFI | PTM: Myristoylation and palmitoylation (probably on one or more of the nearby cysteines at the N-terminus) enable membrane-binding and Golgi apparatus-specific targeting and are essential for efficient packaging.
Function: Plays an important role in the cytoplasmic envelopment of tegument proteins and capsids during th... |
Q55E88 | MNETNYIEENEILIKLGKWEDVYSLPTRMTLESFWYTMEKWSLNPQCMNKSAKKFSLTNKSTYDKNNQQLSNYIFKKNLSGIFLNENEEKEKENYEKEEKEKEKEDENDENENKLKKQKHKHHGCENDEDEDENENIFKQDGSIEKDINTKDINESELAIEYLDDKVETIIYKRHLIPRLLNRDPSIDELVYHRKSSNQCQFIPMLNVIDNARLLPFFYPKVLGFNIIYQQLDSIKDKDLINQLLEKEINDEIEKQKKQKQKQKKNKSNPNKEKKKEEQQEEEIINFKGILKIQVIYFKEFQPKFDKTSKQILEKLNRWG... | Function: Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Catalytic Activity: S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = 2'-O-methyluridine(44) in tRNA(Ser) + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.211
Subcellular Location: Cytoplasm
Sequence Length: 636
Sequence Mass (Da):... |
A0A1Q3EI75 | MSLESLQGNRTLDILYKAEQGGYGVLAQVCYDAQSVIALVRSAERMASPAMIMLFPVTLAYGKGPFLQFCLSIAHQAAVPIAVHLDHATDPEHLELALIMRSLLFMEEHHYSLSTSIQTDEENIALARPYIDRARKYGIAVEVELGRLEGGEAGLRMISDAKLTNQKNADMFMKGTGAVILAPSIGNLHGSYLKPPNFRQDIIQNLRTTFKGRGIPLCLHGTDELPDELFRECIASGMSKFNINSWARDPYLKTFTSALQVGRPLPDAIEEATEMFATPPPGFSQSSLKVNVLNVHRLSTLSNPQLLHTHTSNLVTGDQA... | Cofactor: Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
Function: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or gl... |
A0A1C5G7K5 | MQLVPEGSALMSGRLSSGPSRQVHEEILRPQFIFDMTHLLPHYLAVEVALLFEYERMGVVTGDQRRDITDILGRIDESTLSADPATNMSDTSMAIEQWVHRQLTEPVPTWHVDRSRNDSQATAHALAAREWFGGAAEDLLGLGEAVHRLANATTDMLMPGYTHLQAAQVITPGFYLAALSQQILHNLRRWLATYDSNDLSPLGAGSMAGQQLPWDRHRMAHLLGFAGPVPHALTAVASRSLALEMMAEFSILGAELSRFVTDLMTWGSNEYAFIDLPDELSGISAAMPQKKNFPILERIRGKLAHLGAFGVDIVLAQRST... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
EC: 4.3.2.1
Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Sequence Length: 502
Sequence Mass (Da): 55421
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A0A2M4CKH2 | MAPMVQRYRRLLTISAWIYLVPCSYCPVRKSFLISYRNAFALLLASVFFLSYMTIDFWFVKEFFRRSTPVMMGLVCLDTASFAVLIPCLAMNGFFHRKRFIRLFNALFARDEWMLDWASKGVAANPINHSRFLLAVIIIFSTYYVAPSMPTAVRFQNLFILLRFCVQFGMVEVYCASVNIIKLRMKQLMIVFPMSATKTLVQDSGDRISDRKLAIFFDRYRHYQQQIVHINKCFSIPLLNGILIIVVELCFTCFDVFVGTDLADLGLMNFTIRQIIELVFVFMIVRIATVSHSAAEQVIATTLHDHHS | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 308
Sequence Mass (Da): 35653
Location Topology: Multi-pass membrane protein
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A0A2I7YT99 | HAFVMIFFMVMPIMXGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A1Q3DY30 | MPNNLHILFLDPPQLLHIRPHHQQSPSSEIIAPTPRRHLLESNASQSWLHTPPLSPVSSRGISPTSTRAMSPHSHLTRGTNVAYRSESGMGRRWIRWSHKRGMRSSLIAFIFLAFSLFVPGENTPPMYGDYEAQRHWMEITIHIPIHQWYKYDLQYWGLDYPPLTAYVSWICGIAAHSINPTKSSMGLEEPEGSSSHNQILPLLPYALLNSSMSFFLFSFQVHEKTILLPLMPLMLLFSGATSDSEVYSWGALGSNVAVFSMWPLLKKDGLALSYFSLTLLWNRLIGHDPIKVIYTAFPFNSYVHLLSAGIYAAVIFLHI... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 458
Sequence Mass (Da): 51170
Location Topology: Multi-pass membrane protein
|
A0A1Q3E3I9 | MQFKAIHLRLQPIKDVLRLISASATLGAWIQVDEMLKDAIVPRNMNCITREFRWPCRTSSFRCFIRMEAVLALTKVPCILLATMGLHVTATPPHPPPAKSDQAPSTNWEIIVKQRGVPATIKFICWVAAFAEILLIVTQTLGYQSFTMIVLYPLGMQMRIDQPSIYGGYIRYRCYQELGRMFTFEMTIMKEHKLVTTGPYAWVRHPAYTGVICTISGIVMVHCASGSWLIECKYDYDWSHKTYPEGR | Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.100
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 247
Sequence Mass (Da): 28256
Location To... |
X0PJB1 | MSSIVVVGSQWGDEGKGKITDFFGQDADITARYQGGDNAGHTIVLNGKSYHLQLIPSGIFDQEKYSVIGNGVVVNPKSLINEIDQLKKDGISTDNLRISNRAHVIMPYHILLDGLQEKKKDAKIGTTNKGIGPAYMDKYERIGIRIADLIDKETFEEKLRSALEVKNELLTKIYDVAPLNFDTIFNEYNAYADRIRPYVIDASYLINNALDEHKNVLFEGAQGVMLDVDHGTYPFVTSSNPSASGAAVGTGIGPNRIDNVIGVCKAYTSRLVKVPSQPS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular ... |
C4L498 | MDYGIYGLIIGIIVVVLGGMLGSMLIRRNFYQKIDDLDMRKQSVLSASIPVELQKFKQWPMEGETKEKFDRWHQSWDELVSVHAGQIDEALYRAEEDLDKYRFMKVKADLNATEQLIEELETMVHAMLDEMDEFTTHHTSLMDIVKQDEKELYQFRKTLNSQNHAFGPTYALVEQEIAAAEAKRSEMINLKQVGQVSEAFETGQALSNQVGHIRELIRVIPQFVRTVQVELKQQLQQLRAGHKEMQMDGYALEPLGLMEEIDQAENRREELMVRIERLEFDHFEEDMQQLSSDIDQLFEAFRTEVDARQYVKKEFATIQE... | Function: Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization.
Subcellular Location: Cell membrane
Sequence Length: 576
Sequence Mas... |
A0A975HK78 | MRLSVDFQPFRYTVLGDEFAVPTSRYAFTQSTMLLWNDRVANHYRWPLDLPSSLALFSGQNQSSSGPSVSLAYCGHQFGHFNPSLGDGRAHLVAQLATVDGGVDVQTKGSGPSRFSRGGDGLSAMGPAIREFIMSDAMWHLGVPTTHCLGVLDTHHEVYRQQREAGGLSVRIADSHIRIGSFQYVAMQHDIEKLNTLMELAISRHYGDIKSTGEARVIEFLVAVCQQQARLILQWLRIGFVHGVMNTDNALVSGQTIDYGPCAMMENYSLDTVFSSIDKQGRYAFGQQANIANWNCARLAESLIPLFADEQVAVSKLSEA... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
EC: 2.7.7.108
Catalytic Activity: ATP + L-seryl-[protein] = 3-O-(5'-adenylyl)-L-seryl-[protein] + diphosphate
Sequence Length: 478
Sequence Mass (Da): 53111
|
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